Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Studying "invisible" excited protein states in slow exchange with a major state conformation.

Journal of the American Chemical Society - 16 May 2012

Vallurupalli Pramodh, Bouvignies Guillaume, Kay Lewis E

Abstract excerpt

Ever since its initial development, solution NMR spectroscopy has been used as a tool to study conformational exchange. Although many systems are amenable to relaxation dispersion approaches, cases involving highly skewed populations in slow chemical exchange have, in general, remained recalcitrant to study. Here an experiment to detect and characterize "invisible" excited protein states in slow exchange with a...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Carrier Proteins
Share to Kinetics
Share to Nuclear Magnetic Resonance, Biomolecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Conformation

Share to Protein Folding

Share to Protein Structure, Tertiary

Share to Proteins

Share to Reproducibility of Results

Source

Identifiers

PMID: 22554188
DOI: 10.1021/ja3001419

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Studying "invisible" excited protein states in slow exchange with a major state conformation.PMID 22554188Read ↗

Measurement of methyl group motional parameters of invisible, excited protein states by NMR spectroscopy.Semantic proximity Read ↗

Using CEST NMR to discover previously unobserved states on the free energy surface of proteins: Application to the L99A cavity mutant of T4 lysozyme.Semantic proximity Read ↗

Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences.Semantic proximity Read ↗

Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR.Semantic proximity Read ↗

Solution structure of a minor and transiently formed state of a T4 lysozyme mutant.Semantic proximity Read ↗

Slow exchange in the chromophore of a green fluorescent protein variant.Semantic proximity Read ↗

Side-chain interactions in the folding pathway of a Fyn SH3 domain mutant studied by relaxation dispersion NMR spectroscopy.Semantic proximity Read ↗

Multiquantum Chemical Exchange Saturation Transfer NMR to Quantify Symmetrical Exchange: Application to Rotational Dynamics of the Guanidinium Group in Arginine Side Chains.Semantic proximity Read ↗

Characterizing RNA Excited States Using NMR Relaxation Dispersion.Semantic proximity Read ↗

Amyloid forming human lysozyme intermediates are stabilised by non-native amide-π interactionsSemantic proximity Read ↗

Paramagnetic ions enable tuning of nuclear relaxation rates and provide long-range structural restraints in solid-state NMR of proteins.Semantic proximity Read ↗

Separating degenerate (1)H transitions in methyl group probes for single-quantum (1)H-CPMG relaxation dispersion NMR spectroscopy.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.